RD54_PHYIT
ID RD54_PHYIT Reviewed; 381 AA.
AC D0NBE6;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=RxLR effector protein 54 {ECO:0000303|PubMed:26765567};
DE Flags: Precursor;
GN Name=PexRD54 {ECO:0000303|PubMed:26765567}; ORFNames=PITG_09316;
OS Phytophthora infestans (strain T30-4) (Potato late blight agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=403677;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T30-4;
RX PubMed=19741609; DOI=10.1038/nature08358;
RG The Broad Institute Genome Sequencing Platform;
RA Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M.,
RA Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O.,
RA Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A.,
RA Baxter L., Beynon J., Boevink P.C., Bollmann S.R., Bos J.I., Bulone V.,
RA Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S.,
RA Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S.,
RA Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J.,
RA Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S.,
RA Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P.,
RA Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S.,
RA Nusbaum C.;
RT "Genome sequence and analysis of the Irish potato famine pathogen
RT Phytophthora infestans.";
RL Nature 461:393-398(2009).
RN [2]
RP INTERACTION WITH HOST ATG8CL, FUNCTION, DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=26765567; DOI=10.7554/elife.10856;
RA Dagdas Y.F., Belhaj K., Maqbool A., Chaparro-Garcia A., Pandey P.,
RA Petre B., Tabassum N., Cruz-Mireles N., Hughes R.K., Sklenar J., Win J.,
RA Menke F., Findlay K., Banfield M.J., Kamoun S., Bozkurt T.O.;
RT "An effector of the Irish potato famine pathogen antagonizes a host
RT autophagy cargo receptor.";
RL Elife 5:0-0(2016).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=29932422; DOI=10.7554/elife.37476;
RA Dagdas Y.F., Pandey P., Tumtas Y., Sanguankiattichai N., Belhaj K.,
RA Duggan C., Leary A.Y., Segretin M.E., Contreras M.P., Savage Z.,
RA Khandare V.S., Kamoun S., Bozkurt T.O.;
RT "Host autophagy machinery is diverted to the pathogen interface to mediate
RT focal defense responses against the Irish potato famine pathogen.";
RL Elife 7:0-0(2018).
RN [4]
RP INDUCTION.
RX PubMed=28228125; DOI=10.1186/s12864-017-3585-x;
RA Ah-Fong A.M., Kim K.S., Judelson H.S.;
RT "RNA-seq of life stages of the oomycete Phytophthora infestans reveals
RT dynamic changes in metabolic, signal transduction, and pathogenesis genes
RT and a major role for calcium signaling in development.";
RL BMC Genomics 18:198-198(2017).
RN [5]
RP INDUCTION.
RX PubMed=29312401; DOI=10.3389/fpls.2017.02155;
RA Yin J., Gu B., Huang G., Tian Y., Quan J., Lindqvist-Kreuze H., Shan W.;
RT "Conserved RXLR effector genes of Phytophthora infestans expressed at the
RT early stage of potato infection are suppressive to host defense.";
RL Front. Plant Sci. 8:2155-2155(2017).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 92-381 IN COMPLEX WITH ATG8CL,
RP INTERACTION WITH HOST ATG8CL, AND MUTAGENESIS OF TRP-378; GLU-379 AND
RP VAL-381.
RX PubMed=27458016; DOI=10.1074/jbc.m116.744995;
RA Maqbool A., Hughes R.K., Dagdas Y.F., Tregidgo N., Zess E., Belhaj K.,
RA Round A., Bozkurt T.O., Kamoun S., Banfield M.J.;
RT "Structural basis of host autophagy-related protein 8 (ATG8) binding by the
RT Irish potato famine pathogen effector protein PexRD54.";
RL J. Biol. Chem. 291:20270-20282(2016).
CC -!- FUNCTION: Effector that specifically binds host autophagy protein
CC ATG8CL of the ATG8 family to stimulate autophagosome formation and
CC subsequent autophagy rather than blocking autophagic flux
CC (PubMed:26765567, PubMed:29932422). The pathogen remodels host-microbe
CC interface by co-opting the host autophagy machinery which plays a key
CC role in plant immunity (PubMed:29932422). PexRD54 competes with the
CC autophagy cargo receptor Joka2 to deplete it out of ATG8CL complexes
CC and interferes with Joka2's positive effect on pathogen defense
CC (PubMed:26765567, PubMed:29932422). {ECO:0000269|PubMed:26765567,
CC ECO:0000269|PubMed:29932422}.
CC -!- SUBUNIT: Interacts via its C-terminal AIM with host ATG8CL.
CC {ECO:0000269|PubMed:26765567, ECO:0000269|PubMed:27458016}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26765567}. Host
CC nucleus {ECO:0000269|PubMed:26765567}. Host cytoplasm
CC {ECO:0000269|PubMed:26765567}. Note=Localizes to host autophagosomes
CC across the perimicrobial membrane. {ECO:0000269|PubMed:29932422}.
CC -!- INDUCTION: Expression is induced during host plant infection.
CC {ECO:0000269|PubMed:28228125, ECO:0000269|PubMed:29312401}.
CC -!- DOMAIN: The RxLR-dEER motif acts to carry the protein into the host
CC cell cytoplasm through binding to cell surface phosphatidylinositol-3-
CC phosphate. {ECO:0000305|PubMed:26765567}.
CC -!- DOMAIN: The C-terminal ATG8 interacting motif (AIM) is necessary and
CC sufficient to bind ATG8CL and localize to host autophagosomes.
CC {ECO:0000269|PubMed:26765567, ECO:0000269|PubMed:27458016}.
CC -!- DOMAIN: Contains 5 tandem repeated WY-domains dispensable for the
CC interaction with ATG8CL and which function has still to be determined.
CC {ECO:0000305|PubMed:27458016}.
CC -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Twisting fate - Issue 214 of
CC May 2019;
CC URL="https://web.expasy.org/spotlight/back_issues/214/";
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DR EMBL; DS028131; EEY55375.1; -; Genomic_DNA.
DR RefSeq; XP_002903599.1; XM_002903553.1.
DR PDB; 5L7S; X-ray; 2.90 A; A=92-381.
DR PDBsum; 5L7S; -.
DR AlphaFoldDB; D0NBE6; -.
DR SMR; D0NBE6; -.
DR EnsemblProtists; PITG_09316T0; PITG_09316T0; PITG_09316.
DR GeneID; 9461793; -.
DR KEGG; pif:PITG_09316; -.
DR VEuPathDB; FungiDB:PITG_09316; -.
DR eggNOG; ENOG502T0RF; Eukaryota.
DR HOGENOM; CLU_044421_1_0_1; -.
DR InParanoid; D0NBE6; -.
DR OMA; RDTAGND; -.
DR OrthoDB; 1258663at2759; -.
DR Proteomes; UP000006643; Partially assembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR InterPro; IPR040786; RXLR_WY.
DR Pfam; PF18634; RXLR_WY; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Host cytoplasm; Host nucleus; Reference proteome; Repeat;
KW Secreted; Signal; Virulence.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..381
FT /note="RxLR effector protein 54"
FT /id="PRO_5003012478"
FT REGION 97..150
FT /note="WY-domain 1"
FT /evidence="ECO:0000305|PubMed:27458016"
FT REGION 151..198
FT /note="WY-domain 2"
FT /evidence="ECO:0000305|PubMed:27458016"
FT REGION 199..247
FT /note="WY-domain 3"
FT /evidence="ECO:0000305|PubMed:27458016"
FT REGION 251..299
FT /note="WY-domain 4"
FT /evidence="ECO:0000305|PubMed:27458016"
FT REGION 302..354
FT /note="WY-domain 5"
FT /evidence="ECO:0000305|PubMed:27458016"
FT MOTIF 57..75
FT /note="RxLR-dEER"
FT /evidence="ECO:0000305|PubMed:26765567"
FT MOTIF 372..381
FT /note="ATG8 interacting motif"
FT /evidence="ECO:0000305|PubMed:26765567,
FT ECO:0000305|PubMed:27458016"
FT MUTAGEN 378
FT /note="W->A,V,T,S,R,Q,P,N,M,K,H,G,E,D,C: Impairs the
FT interaction with ATG8CL."
FT /evidence="ECO:0000269|PubMed:27458016"
FT MUTAGEN 379
FT /note="E->P: Impairs the interaction with ATG8CL."
FT /evidence="ECO:0000269|PubMed:27458016"
FT MUTAGEN 381
FT /note="V->A,W,S,R,Q,P,N,M,K,H,G,F,E,D,C: Impairs the
FT interaction with ATG8CL."
FT /evidence="ECO:0000269|PubMed:27458016"
FT HELIX 98..109
FT /evidence="ECO:0007829|PDB:5L7S"
FT HELIX 113..119
FT /evidence="ECO:0007829|PDB:5L7S"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:5L7S"
FT HELIX 133..149
FT /evidence="ECO:0007829|PDB:5L7S"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:5L7S"
FT HELIX 156..164
FT /evidence="ECO:0007829|PDB:5L7S"
FT HELIX 169..180
FT /evidence="ECO:0007829|PDB:5L7S"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:5L7S"
FT HELIX 186..195
FT /evidence="ECO:0007829|PDB:5L7S"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:5L7S"
FT HELIX 211..217
FT /evidence="ECO:0007829|PDB:5L7S"
FT HELIX 220..229
FT /evidence="ECO:0007829|PDB:5L7S"
FT HELIX 231..244
FT /evidence="ECO:0007829|PDB:5L7S"
FT HELIX 254..262
FT /evidence="ECO:0007829|PDB:5L7S"
FT HELIX 268..278
FT /evidence="ECO:0007829|PDB:5L7S"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:5L7S"
FT HELIX 285..296
FT /evidence="ECO:0007829|PDB:5L7S"
FT HELIX 302..312
FT /evidence="ECO:0007829|PDB:5L7S"
FT HELIX 317..324
FT /evidence="ECO:0007829|PDB:5L7S"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:5L7S"
FT HELIX 338..353
FT /evidence="ECO:0007829|PDB:5L7S"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:5L7S"
FT HELIX 361..368
FT /evidence="ECO:0007829|PDB:5L7S"
SQ SEQUENCE 381 AA; 43859 MW; 0186EADB58F4F3D7 CRC64;
MRFQSIMMLT ITCAGTCLAE GLAPSDQAYR PTMTGLKSRL NDPRPLSTAT IATSSERFLR
FDTVARDTAG NDEERVGPSW LAKVDGLMHK MVTSSLSAEE AQLKVWIQSQ IHPRELFGVL
SLGKRAAKLD DNPDFVQWLR LVKDFRANNG NQAFSDLDIY YLLLKTNSPE QLKLLFETLR
HTPGMTKIGA SMEKSLSGNW IRKALEQDTY PTIVYNTLRL KDAGTKLDDT PMFRQWLEYV
EKYWNKNAGA FFGDTQMLTL FQKTMTEEED IIKLVHMLRN NPGMKSHADK LERYLLLTSE
SSHKTMADVW LKARETPEEV FRILRLAEKQ TAAADDNRML NLWLRYTQTY RDKIDKNAFS
DAEALQFFRK AKPLDFDWEI V
